Some properties of pea cholinesterase and its activity in plant parts at different growth stages

Abstract

Cholinesterase activity was studied in 2 to 10-week-old pea plants cultivated under artificial illumination. Free and membrane-bound forms of the enzyme were separated by extracting the enzyme from pea shoots with buffers differing in ionic strength. The ratio of the free cholinesterase to the membrane-bound one fluctuated between 1 : 1 and 1 : 2.5. The free cholinesterase was inhibited by neostigmine (0.1mmoll^-1) by 50%, the membrane-bound enzyme by 90%. The pH optimum of cholinesterase activity was 8.5, the temperature optimum 37 °C. The enzyme activity was increased by some cations in this order: Mg²⁺ < < K⁺. The K^m value for the substrate S-acetylthiocholine iodide was 250 μmoll^-1, the enzyme activity being inhibited by concentrations higher than 3 mmoll^-1 of this substrate.

The activity of the membrane-bound enzyme was demonstrated in the roots, leaves, stems, fruits, seeds and carpels, but could not be reliably detected in the blossoms. The highest activity expressed per fresh matter was found in older leaves and in the fruits, the lowest in the roots and stems. Cholinesterase activity in plant parts markedly varied during the investigated growth period.